Abstract
Abstract The immune system surveys the body for foreign or mutated structures with the help of the human leukocyte antigen class I (HLA-I) protein complex, which displays protein fragments called peptides on the cell surface. The genes encoding the HLA-I heavy chain in humans are highly variable, which results in predisposition to or protection from diseases based on individual HLA-I variants. We have observed that sub-optimal assembly conditions for certain HLA-B variants produce peptide-deficient molecules on the cell surface. The monocyte immune cell type overcomes this deficiency in assembly, reversing the previously observed trends. Intracellular HLA-B accumulates in monocytes and monocyte-derived dendritic cells (moDCs) in endo-lysosomal compartments, a predicted location for supplemental peptide assembly. Current findings suggest that certain HLA-B variants are better able to efficiently assemble with intracellular and extracellular antigens in the endolysosomal compartments, conferring a selective advantage in infection conditions where traditional antigen presentation is blocked.
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